| Literature DB >> 19331323 |
Stefano V Gullà1, Gaurav Sharma, Peter Borbat, Jack H Freed, Harishchandra Ghimire, Monica R Benedikt, Natasha L Holt, Gary A Lorigan, Kaushal Rege, Constantinos Mavroidis, David E Budil.
Abstract
A new method for measuring forces between small protein domains based on double electron-electron resonance (DEER) spectroscopy is demonstrated using a model peptide derived from the alpha-helical coiled-coil leucine zipper of yeast transcriptional activator GCN4. The equilibrium distribution of distances between two nitroxide spin labels rigidly attached to the helices of the dimer was determined by DEER and yielded a closing force of 100 +/- 10 pN between monomers, in excellent agreement with theoretical predictions.Entities:
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Year: 2009 PMID: 19331323 PMCID: PMC2888838 DOI: 10.1021/ja900230w
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419